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P37617

- ATZN_ECOLI

UniProt

P37617 - ATZN_ECOLI

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Protein
Lead, cadmium, zinc and mercury-transporting ATPase
Gene
zntA, yhhO, b3469, JW3434
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in export of lead, cadmium, zinc and mercury.

Catalytic activityi

ATP + H2O + Cd2+(In) = ADP + phosphate + Cd2+(Out).
ATP + H2O + Zn2+(In) = ADP + phosphate + Zn2+(Out).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi58 – 581Zinc
Metal bindingi59 – 591Zinc
Metal bindingi62 – 621Zinc
Active sitei436 – 43614-aspartylphosphate intermediate By similarity
Metal bindingi628 – 6281Magnesium By similarity
Metal bindingi632 – 6321Magnesium By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATPase activity Source: EcoliWiki
  3. cadmium-exporting ATPase activity Source: EcoCyc
  4. cobalt ion transmembrane transporter activity Source: EcoCyc
  5. lead ion transmembrane transporter activity Source: EcoCyc
  6. metal ion binding Source: UniProtKB-KW
  7. nickel cation transmembrane transporter activity Source: EcoCyc
  8. zinc-exporting ATPase activity Source: EcoCyc
Complete GO annotation...

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. cadmium ion transmembrane transport Source: GOC
  3. cobalt ion transport Source: EcoCyc
  4. detoxification of zinc ion Source: EcoliWiki
  5. lead ion transport Source: EcoCyc
  6. nickel cation transmembrane transport Source: GOC
  7. response to cadmium ion Source: EcoliWiki
  8. zinc ion transmembrane transport Source: GOC
  9. zinc ion transport Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Cadmium, Magnesium, Mercury, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:YHHO-MONOMER.
ECOL316407:JW3434-MONOMER.
MetaCyc:YHHO-MONOMER.
SABIO-RKP37617.

Protein family/group databases

TCDBi3.A.3.6.2. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Lead, cadmium, zinc and mercury-transporting ATPase (EC:3.6.3.3, EC:3.6.3.5)
Gene namesi
Name:zntA
Synonyms:yhhO
Ordered Locus Names:b3469, JW3434
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG12215. zntA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 124124Periplasmic Reviewed prediction
Add
BLAST
Transmembranei125 – 14521Helical; Reviewed prediction
Add
BLAST
Topological domaini146 – 19146Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei192 – 21221Helical; Reviewed prediction
Add
BLAST
Topological domaini213 – 356144Periplasmic Reviewed prediction
Add
BLAST
Transmembranei357 – 37721Helical; Reviewed prediction
Add
BLAST
Topological domaini378 – 3836Cytoplasmic Reviewed prediction
Transmembranei384 – 40421Helical; Reviewed prediction
Add
BLAST
Topological domaini405 – 46157Periplasmic Reviewed prediction
Add
BLAST
Transmembranei462 – 48221Helical; Reviewed prediction
Add
BLAST
Topological domaini483 – 632150Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei633 – 65321Helical; Reviewed prediction
Add
BLAST
Topological domaini654 – 69340Periplasmic Reviewed prediction
Add
BLAST
Transmembranei694 – 71421Helical; Reviewed prediction
Add
BLAST
Topological domaini715 – 73218Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: EcoCyc
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 732732Lead, cadmium, zinc and mercury-transporting ATPase
PRO_0000046332Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP37617.
PRIDEiP37617.

Expressioni

Gene expression databases

GenevestigatoriP37617.

Interactioni

Protein-protein interaction databases

DIPiDIP-12947N.
IntActiP37617. 8 interactions.
MINTiMINT-1256950.
STRINGi511145.b3469.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi48 – 569
Helixi62 – 7110
Beta strandi73 – 8210
Turni83 – 864
Beta strandi87 – 948
Helixi97 – 10711
Beta strandi110 – 1134

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MWYNMR-A46-118[»]
1MWZNMR-A46-118[»]
ProteinModelPortaliP37617.
SMRiP37617. Positions 46-732.

Miscellaneous databases

EvolutionaryTraceiP37617.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 11365HMA
Add
BLAST

Sequence similaritiesi

Contains 1 HMA domain.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2217.
HOGENOMiHOG000250399.
KOiK01534.
OMAiSGMDCPS.
OrthoDBiEOG6742RM.
PhylomeDBiP37617.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR027256. Cation_transp_P-typ_ATPase_IB.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
PR00120. HATPASE.
SUPFAMiSSF55008. SSF55008. 1 hit.
SSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37617-1 [UniParc]FASTAAdd to Basket

« Hide

MSTPDNHGKK APQFAAFKPL TTVQNANDCC CDGACSSTPT LSENVSGTRY    50
SWKVSGMDCA ACARKVENAV RQLAGVNQVQ VLFATEKLVV DADNDIRAQV 100
ESALQKAGYS LRDEQAAEEP QASRLKENLP LITLIVMMAI SWGLEQFNHP 150
FGQLAFIATT LVGLYPIARQ ALRLIKSGSY FAIETLMSVA AIGALFIGAT 200
AEAAMVLLLF LIGERLEGWA ASRARQGVSA LMALKPETAT RLRKGEREEV 250
AINSLRPGDV IEVAAGGRLP ADGKLLSPFA SFDESALTGE SIPVERATGD 300
KVPAGATSVD RLVTLEVLSE PGASAIDRIL KLIEEAEERR APIERFIDRF 350
SRIYTPAIMA VALLVTLVPP LLFAASWQEW IYKGLTLLLI GCPCALVIST 400
PAAITSGLAA AARRGALIKG GAALEQLGRV TQVAFDKTGT LTVGKPRVTA 450
IHPATGISES ELLTLAAAVE QGATHPLAQA IVREAQVAEL AIPTAESQRA 500
LVGSGIEAQV NGERVLICAA GKHPADAFTG LINELESAGQ TVVLVVRNDD 550
VLGVIALQDT LRADAATAIS ELNALGVKGV ILTGDNPRAA AAIAGELGLE 600
FKAGLLPEDK VKAVTELNQH APLAMVGDGI NDAPAMKAAA IGIAMGSGTD 650
VALETADAAL THNHLRGLVQ MIELARATHA NIRQNITIAL GLKGIFLVTT 700
LLGMTGLWLA VLADTGATVL VTANALRLLR RR 732
Length:732
Mass (Da):76,840
Last modified:October 1, 1994 - v1
Checksum:i25476EA830786465
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00039 Genomic DNA. Translation: AAB18444.1.
U00096 Genomic DNA. Translation: AAC76494.1.
AP009048 Genomic DNA. Translation: BAE77824.1.
PIRiS47688.
RefSeqiNP_417926.1. NC_000913.3.
YP_491965.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76494; AAC76494; b3469.
BAE77824; BAE77824; BAE77824.
GeneIDi12933927.
947972.
KEGGiecj:Y75_p3709.
eco:b3469.
PATRICi32122382. VBIEscCol129921_3568.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00039 Genomic DNA. Translation: AAB18444.1 .
U00096 Genomic DNA. Translation: AAC76494.1 .
AP009048 Genomic DNA. Translation: BAE77824.1 .
PIRi S47688.
RefSeqi NP_417926.1. NC_000913.3.
YP_491965.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MWY NMR - A 46-118 [» ]
1MWZ NMR - A 46-118 [» ]
ProteinModelPortali P37617.
SMRi P37617. Positions 46-732.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-12947N.
IntActi P37617. 8 interactions.
MINTi MINT-1256950.
STRINGi 511145.b3469.

Protein family/group databases

TCDBi 3.A.3.6.2. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbi P37617.
PRIDEi P37617.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76494 ; AAC76494 ; b3469 .
BAE77824 ; BAE77824 ; BAE77824 .
GeneIDi 12933927.
947972.
KEGGi ecj:Y75_p3709.
eco:b3469.
PATRICi 32122382. VBIEscCol129921_3568.

Organism-specific databases

EchoBASEi EB2129.
EcoGenei EG12215. zntA.

Phylogenomic databases

eggNOGi COG2217.
HOGENOMi HOG000250399.
KOi K01534.
OMAi SGMDCPS.
OrthoDBi EOG6742RM.
PhylomeDBi P37617.

Enzyme and pathway databases

BioCyci EcoCyc:YHHO-MONOMER.
ECOL316407:JW3434-MONOMER.
MetaCyc:YHHO-MONOMER.
SABIO-RK P37617.

Miscellaneous databases

EvolutionaryTracei P37617.
PROi P37617.

Gene expression databases

Genevestigatori P37617.

Family and domain databases

Gene3Di 2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProi IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR027256. Cation_transp_P-typ_ATPase_IB.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view ]
Pfami PF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view ]
PRINTSi PR00119. CATATPASE.
PR00120. HATPASE.
SUPFAMi SSF55008. SSF55008. 1 hit.
SSF56784. SSF56784. 2 hits.
TIGRFAMsi TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase."
    Rensing C., Mitra B., Rosen B.P.
    Proc. Natl. Acad. Sci. U.S.A. 94:14326-14331(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase."
    Beard S.J., Hashim R., Membrillo-Hernandez J., Hughes M.N., Poole R.K.
    Mol. Microbiol. 25:883-891(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli."
    Sharma R., Rensing C., Rosen B.P., Mitra B.
    J. Biol. Chem. 275:3873-3878(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  8. "A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118)."
    Banci L., Bertini I., Ciofi-Baffoni S., Finney L.A., Outten C.E., O'Halloran T.V.
    J. Mol. Biol. 323:883-897(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 46-118 IN APO AND ZINC-BOUND FORMS.

Entry informationi

Entry nameiATZN_ECOLI
AccessioniPrimary (citable) accession number: P37617
Secondary accession number(s): Q2M7D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi